Try it on paper first. A hint, the key idea and the worked solution are here when you need them.
Dilip dialyses a purified enzyme, which removes small molecules but keeps the protein. The enzyme loses all its activity. When he adds a small molecule from boiled yeast extract, the activity returns. A different small molecule does not bring it back. A second enzyme keeps its full activity after dialysis. (a) What did the first enzyme need? (b) Which kind of cofactor is likely, and why could dialysis remove it? (c) If the second enzyme needs a cofactor at all, which kind is it likely to be?
Six classes: oxidoreductases (hydrogen, oxidation and reduction), transferases (another group), hydrolases (water), lyases (other breaking, double bond left), isomerases (rearranging), ligases (joining, with ATP). Apoenzyme + cofactor = holoenzyme. Cofactors: prosthetic group (tight, haem), coenzyme (loose, NAD from niacin), metal ion (zinc).
Have you tried it?
Work it out on paper first. It is fine to get stuck or make a mistake: that is how we learn. When you are ready, go through the solution one step at a time, and check each step against your own.
Step 1. What it needed. It needed a cofactor, a small non-protein molecule. Without it, the apoenzyme has no activity. The small molecule from the extract supplied it.
Step 2. Which kind. It was removed by dialysis, so it was bound loosely. A loosely bound organic molecule is a coenzyme. (A metal ion can also be removed this way.) Heating the extract did not destroy it, as a small molecule is not denatured.
Step 3. The second enzyme. Dialysis did not remove anything it needed. Any cofactor it has must be bound tightly. That is a prosthetic group, such as haem.
Answer: (a) a cofactor, (b) a coenzyme, loosely bound and small, (c) a prosthetic group.
Log in to join the discussion.
Loading…